HEADER IMMUNE SYSTEM 13-AUG-15 5D71
TITLE CRYSTAL STRUCTURE OF MOR04302, A NEUTRALIZING ANTI-HUMAN GM-CSF
TITLE 2 ANTIBODY FAB FRAGMENT IN COMPLEX WITH HUMAN GM-CSF
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GRANULOCYTE-MACROPHAGE COLONY-STIMULATING FACTOR;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: GM-CSF,COLONY-STIMULATING FACTOR,CSF,MOLGRAMOSTIN,
COMPND 5 SARGRAMOSTIM;
COMPND 6 ENGINEERED: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: IMMUNGLOBULIN G1 FAB FRAGMENT, HEAVY CHAIN;
COMPND 9 CHAIN: H;
COMPND 10 ENGINEERED: YES;
COMPND 11 MOL_ID: 3;
COMPND 12 MOLECULE: IMMUNGLOBULIN G1 FAB FRAGMENT, LIGHT CHAIN;
COMPND 13 CHAIN: L;
COMPND 14 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: CSF2, GMCSF;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 10 ORGANISM_COMMON: HUMAN;
SOURCE 11 ORGANISM_TAXID: 9606;
SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 16 ORGANISM_COMMON: HUMAN;
SOURCE 17 ORGANISM_TAXID: 9606;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS GM-CSF, AFFINITY MATURATION, PHAGE DISPLAY, CYTOKINE, ANTIBODY,
KEYWDS 2 PROTEROS BIOSTRUCTURES GMBH, IMMUNE SYSTEM
EXPDTA X-RAY DIFFRACTION
AUTHOR R.EYLENSTEIN,D.WEINFURTNER,S.STEIDL,J.BOETTCHER,M.AUGUSTIN
REVDAT 4 10-JAN-24 5D71 1 REMARK
REVDAT 3 13-JAN-16 5D71 1 JRNL
REVDAT 2 28-OCT-15 5D71 1 JRNL
REVDAT 1 14-OCT-15 5D71 0
JRNL AUTH R.EYLENSTEIN,D.WEINFURTNER,S.HARTLE,R.STROHNER,J.BOTTCHER,
JRNL AUTH 2 M.AUGUSTIN,R.OSTENDORP,S.STEIDL
JRNL TITL MOLECULAR BASIS OF IN VITRO AFFINITY MATURATION AND
JRNL TITL 2 FUNCTIONAL EVOLUTION OF A NEUTRALIZING ANTI-HUMAN GM-CSF
JRNL TITL 3 ANTIBODY.
JRNL REF MABS V. 8 176 2016
JRNL REFN ESSN 1942-0870
JRNL PMID 26406987
JRNL DOI 10.1080/19420862.2015.1099774
REMARK 2
REMARK 2 RESOLUTION. 2.25 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.2.0005
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 112.20
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 30163
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.181
REMARK 3 R VALUE (WORKING SET) : 0.180
REMARK 3 FREE R VALUE : 0.219
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.400
REMARK 3 FREE R VALUE TEST SET COUNT : 1393
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.25
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.31
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2216
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.74
REMARK 3 BIN R VALUE (WORKING SET) : 0.2330
REMARK 3 BIN FREE R VALUE SET COUNT : 95
REMARK 3 BIN FREE R VALUE : 0.3280
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3969
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 17
REMARK 3 SOLVENT ATOMS : 198
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 51.36
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 0.222
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.184
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.131
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.026
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.962
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.945
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3962 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): 3443 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 5416 ; 1.314 ; 1.950
REMARK 3 BOND ANGLES OTHERS (DEGREES): 7997 ; 0.934 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 522 ; 6.727 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 137 ;34.294 ;24.161
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 564 ;12.315 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 12 ;14.815 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 615 ; 0.076 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 4461 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 776 ; 0.002 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 549 ; 0.173 ; 0.200
REMARK 3 NON-BONDED CONTACTS OTHERS (A): 2967 ; 0.157 ; 0.200
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 1845 ; 0.162 ; 0.200
REMARK 3 NON-BONDED TORSION OTHERS (A): 2132 ; 0.076 ; 0.200
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 183 ; 0.109 ; 0.200
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): 4 ; 0.077 ; 0.200
REMARK 3 SYMMETRY VDW OTHERS (A): 28 ; 0.190 ; 0.200
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): 12 ; 0.144 ; 0.200
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3320 ; 2.062 ; 2.000
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1066 ; 0.492 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4196 ; 2.689 ; 3.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1622 ; 3.913 ; 4.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 1220 ; 5.007 ; 6.000
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 5
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 122
REMARK 3 ORIGIN FOR THE GROUP (A): 91.187 108.977 34.661
REMARK 3 T TENSOR
REMARK 3 T11: 0.0216 T22: -0.0425
REMARK 3 T33: 0.0555 T12: 0.0965
REMARK 3 T13: -0.0204 T23: -0.0063
REMARK 3 L TENSOR
REMARK 3 L11: 2.4699 L22: 2.0584
REMARK 3 L33: 6.5508 L12: -1.0334
REMARK 3 L13: -0.3656 L23: -0.4425
REMARK 3 S TENSOR
REMARK 3 S11: -0.0120 S12: -0.2952 S13: -0.3129
REMARK 3 S21: 0.4197 S22: 0.0207 S23: 0.0893
REMARK 3 S31: -0.0250 S32: 0.0590 S33: -0.0088
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 1 L 105
REMARK 3 ORIGIN FOR THE GROUP (A): 99.169 92.138 12.929
REMARK 3 T TENSOR
REMARK 3 T11: -0.1906 T22: -0.0661
REMARK 3 T33: -0.1250 T12: 0.0336
REMARK 3 T13: 0.0159 T23: 0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.8378 L22: 6.0767
REMARK 3 L33: 2.3853 L12: -1.6438
REMARK 3 L13: 0.1829 L23: 1.8522
REMARK 3 S TENSOR
REMARK 3 S11: -0.1806 S12: -0.2352 S13: 0.0381
REMARK 3 S21: 0.1741 S22: 0.1760 S23: 0.1205
REMARK 3 S31: 0.0853 S32: -0.1685 S33: 0.0045
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : L 108 L 209
REMARK 3 ORIGIN FOR THE GROUP (A): 112.602 87.005 -14.466
REMARK 3 T TENSOR
REMARK 3 T11: -0.1603 T22: -0.1064
REMARK 3 T33: -0.1575 T12: -0.0597
REMARK 3 T13: -0.0340 T23: -0.0094
REMARK 3 L TENSOR
REMARK 3 L11: 2.9113 L22: 1.9932
REMARK 3 L33: 6.0907 L12: 0.7815
REMARK 3 L13: -1.1095 L23: -1.5899
REMARK 3 S TENSOR
REMARK 3 S11: -0.1068 S12: 0.1265 S13: -0.0097
REMARK 3 S21: -0.1204 S22: 0.0877 S23: -0.0424
REMARK 3 S31: 0.2459 S32: -0.1660 S33: 0.0190
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 1 H 105
REMARK 3 ORIGIN FOR THE GROUP (A): 87.512 108.617 2.606
REMARK 3 T TENSOR
REMARK 3 T11: -0.1166 T22: -0.1059
REMARK 3 T33: -0.0491 T12: 0.0431
REMARK 3 T13: -0.0864 T23: -0.0148
REMARK 3 L TENSOR
REMARK 3 L11: 1.5295 L22: 3.0086
REMARK 3 L33: 2.7998 L12: -0.8520
REMARK 3 L13: -0.6657 L23: 0.3536
REMARK 3 S TENSOR
REMARK 3 S11: -0.1412 S12: 0.0579 S13: 0.0237
REMARK 3 S21: -0.3016 S22: 0.0956 S23: 0.2669
REMARK 3 S31: -0.1341 S32: -0.1749 S33: 0.0457
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 108 H 213
REMARK 3 ORIGIN FOR THE GROUP (A): 99.976 85.497 -24.063
REMARK 3 T TENSOR
REMARK 3 T11: -0.1127 T22: -0.0679
REMARK 3 T33: -0.0185 T12: -0.0674
REMARK 3 T13: -0.0863 T23: -0.0291
REMARK 3 L TENSOR
REMARK 3 L11: 4.8494 L22: 4.4550
REMARK 3 L33: 3.8318 L12: -2.4841
REMARK 3 L13: 0.3965 L23: 0.1730
REMARK 3 S TENSOR
REMARK 3 S11: 0.2227 S12: 0.3366 S13: -0.7012
REMARK 3 S21: -0.1139 S22: -0.0896 S23: -0.0130
REMARK 3 S31: 0.3240 S32: 0.3074 S33: -0.1331
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : BABINET MODEL WITH MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 5D71 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 13-AUG-15.
REMARK 100 THE DEPOSITION ID IS D_1000212658.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JAN-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 4.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 31568
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.250
REMARK 200 RESOLUTION RANGE LOW (A) : 112.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 24.90
REMARK 200 R MERGE (I) : 0.07400
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 30.3300
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.39
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.3
REMARK 200 DATA REDUNDANCY IN SHELL : 24.30
REMARK 200 R MERGE FOR SHELL (I) : 0.66000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 2GMF
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.20
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.57
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM SODIUM ACETATE, PH 4.0-4.3, 39
REMARK 280 -42 % (W/V) PEG 400, 35 MG/ML PROTEIN, PH 4.2, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 21 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z+1/2,-X+1/2,-Y
REMARK 290 7555 -Z+1/2,-X,Y+1/2
REMARK 290 8555 -Z,X+1/2,-Y+1/2
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z+1/2,-X+1/2
REMARK 290 11555 Y+1/2,-Z+1/2,-X
REMARK 290 12555 -Y+1/2,-Z,X+1/2
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X,-Y+1/2,Z
REMARK 290 15555 -X+1/2,Y,-Z
REMARK 290 16555 X,-Y,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z,-X,-Y+1/2
REMARK 290 19555 -Z,-X+1/2,Y
REMARK 290 20555 -Z+1/2,X,-Y
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z,-X
REMARK 290 23555 Y,-Z,-X+1/2
REMARK 290 24555 -Y,-Z+1/2,X
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 79.34000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 79.34000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 79.34000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 79.34000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 79.34000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 79.34000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 79.34000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 79.34000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 79.34000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 79.34000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 79.34000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 79.34000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 79.34000
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 79.34000
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 79.34000
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 79.34000
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 79.34000
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 79.34000
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 79.34000
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 79.34000
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 79.34000
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 79.34000
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 79.34000
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 79.34000
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 79.34000
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 5440 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 24570 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -59.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -16
REMARK 465 TRP A -15
REMARK 465 LEU A -14
REMARK 465 GLN A -13
REMARK 465 SER A -12
REMARK 465 LEU A -11
REMARK 465 LEU A -10
REMARK 465 LEU A -9
REMARK 465 LEU A -8
REMARK 465 GLY A -7
REMARK 465 THR A -6
REMARK 465 VAL A -5
REMARK 465 ALA A -4
REMARK 465 CYS A -3
REMARK 465 SER A -2
REMARK 465 ILE A -1
REMARK 465 SER A 0
REMARK 465 ALA A 1
REMARK 465 PRO A 2
REMARK 465 ALA A 3
REMARK 465 ARG A 4
REMARK 465 SER A 5
REMARK 465 PRO A 6
REMARK 465 SER A 7
REMARK 465 PRO A 8
REMARK 465 GLU A 123
REMARK 465 PRO A 124
REMARK 465 VAL A 125
REMARK 465 GLN A 126
REMARK 465 GLU A 127
REMARK 465 LYS H 129
REMARK 465 SER H 130
REMARK 465 THR H 131
REMARK 465 SER H 132
REMARK 465 LYS H 214
REMARK 465 SER H 215
REMARK 465 GLU H 216
REMARK 465 PHE H 217
REMARK 465 ASP H 218
REMARK 465 TYR H 219
REMARK 465 LYS H 220
REMARK 465 ASP H 221
REMARK 465 ASP H 222
REMARK 465 ASP H 223
REMARK 465 ASP H 224
REMARK 465 LYS H 225
REMARK 465 GLY H 226
REMARK 465 ALA H 227
REMARK 465 PRO H 228
REMARK 465 HIS H 229
REMARK 465 HIS H 230
REMARK 465 HIS H 231
REMARK 465 HIS H 232
REMARK 465 HIS H 233
REMARK 465 HIS H 234
REMARK 465 TYR L 51
REMARK 465 LYS L 52
REMARK 465 LYS L 53
REMARK 465 ARG L 54
REMARK 465 PRO L 55
REMARK 465 SER L 56
REMARK 465 GLY L 57
REMARK 465 ILE L 58
REMARK 465 PRO L 59
REMARK 465 GLU L 210
REMARK 465 ALA L 211
REMARK 480
REMARK 480 ZERO OCCUPANCY ATOM
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 480 M RES C SSEQI ATOMS
REMARK 480 SER A 9 OG
REMARK 480 LEU A 28 CD1 CD2
REMARK 480 ARG A 30 CG CD NE CZ NH1 NH2
REMARK 480 ASP A 31 CB CG OD1 OD2
REMARK 480 THR A 32 CG2
REMARK 480 GLU A 35 OE1 OE2
REMARK 480 GLU A 41 CD OE1 OE2
REMARK 480 GLU A 45 CG CD OE1 OE2
REMARK 480 MET A 46 CE
REMARK 480 LEU A 49 CD1
REMARK 480 GLN A 50 OE1 NE2
REMARK 480 GLU A 51 CG CD OE1 OE2
REMARK 480 LYS A 63 CG CD CE NZ
REMARK 480 ARG A 67 CG CD NE CZ NH1 NH2
REMARK 480 LYS A 72 CD CE NZ
REMARK 480 LYS A 74 CG CD CE NZ
REMARK 480 LYS A 85 CD CE NZ
REMARK 480 GLN A 99 CG CD OE1 NE2
REMARK 480 LYS A 107 CE NZ
REMARK 480 LYS A 111 CD CE NZ
REMARK 480 LEU A 115 CD1 CD2
REMARK 480 VAL A 116 CG1 CG2
REMARK 480 ILE A 117 CD1
REMARK 480 GLN H 1 CG CD OE1 NE2
REMARK 480 GLN H 3 OE1 NE2
REMARK 480 LYS H 43 CE NZ
REMARK 480 GLU H 56 OE1 OE2
REMARK 480 LYS H 64 CE NZ
REMARK 480 LYS H 75 CE NZ
REMARK 480 LYS H 117 NZ
REMARK 480 SER H 128 OG
REMARK 480 LYS H 143 NZ
REMARK 480 VAL H 182 CG2
REMARK 480 SER H 188 OG
REMARK 480 LEU H 189 CB CG CD1 CD2
REMARK 480 THR H 191 OG1 CG2
REMARK 480 GLN H 192 CD OE1 NE2
REMARK 480 ILE H 195 CD1
REMARK 480 LYS H 201 NZ
REMARK 480 LYS H 206 NZ
REMARK 480 LYS H 210 CD CE NZ
REMARK 480 GLU H 212 OE1 OE2
REMARK 480 ASP L 26 OD1 OD2
REMARK 480 ILE L 28 CD1
REMARK 480 GLU L 60 CG CD OE1 OE2
REMARK 480 GLU L 81 CG CD OE1 OE2
REMARK 480 ASP L 93 OD1 OD2
REMARK 480 LYS L 94 NZ
REMARK 480 GLN L 126 CD OE1 NE2
REMARK 480 LYS L 129 CD CE NZ
REMARK 480 SER L 153 OG
REMARK 480 LYS L 156 CD CE NZ
REMARK 480 LYS L 171 NZ
REMARK 480 GLU L 183 CD OE1 OE2
REMARK 480 LYS L 186 CD CE NZ
REMARK 480 LYS L 204 NZ
REMARK 480 THR L 209 OG1 CG2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 GLU A 35 CD GLU A 35 OE1 -0.078
REMARK 500 GLU H 56 CD GLU H 56 OE1 -0.114
REMARK 500 GLU H 56 CD GLU H 56 OE2 0.071
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 VAL A 116 CA - CB - CG2 ANGL. DEV. = 9.6 DEGREES
REMARK 500 CYS H 92 CA - CB - SG ANGL. DEV. = 6.7 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 GLU A 51 71.26 -150.01
REMARK 500 ASP H 144 63.43 65.66
REMARK 500 THR H 160 -40.64 -132.38
REMARK 500 ASP L 151 -108.67 49.02
REMARK 500 ASP L 151 -109.03 49.02
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG H 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 L 302
DBREF 5D71 A -16 110 UNP P04141 CSF2_HUMAN 1 127
DBREF 5D71 H 1 234 PDB 5D71 5D71 1 234
DBREF 5D71 L 1 211 PDB 5D71 5D71 1 211
SEQADV 5D71 LYS A 111 UNP P04141 EXPRESSION TAG
SEQADV 5D71 ASP A 112 UNP P04141 EXPRESSION TAG
SEQADV 5D71 PHE A 113 UNP P04141 EXPRESSION TAG
SEQADV 5D71 LEU A 114 UNP P04141 EXPRESSION TAG
SEQADV 5D71 LEU A 115 UNP P04141 EXPRESSION TAG
SEQADV 5D71 VAL A 116 UNP P04141 EXPRESSION TAG
SEQADV 5D71 ILE A 117 UNP P04141 EXPRESSION TAG
SEQADV 5D71 PRO A 118 UNP P04141 EXPRESSION TAG
SEQADV 5D71 PHE A 119 UNP P04141 EXPRESSION TAG
SEQADV 5D71 ASP A 120 UNP P04141 EXPRESSION TAG
SEQADV 5D71 CYS A 121 UNP P04141 EXPRESSION TAG
SEQADV 5D71 TRP A 122 UNP P04141 EXPRESSION TAG
SEQADV 5D71 GLU A 123 UNP P04141 EXPRESSION TAG
SEQADV 5D71 PRO A 124 UNP P04141 EXPRESSION TAG
SEQADV 5D71 VAL A 125 UNP P04141 EXPRESSION TAG
SEQADV 5D71 GLN A 126 UNP P04141 EXPRESSION TAG
SEQADV 5D71 GLU A 127 UNP P04141 EXPRESSION TAG
SEQRES 1 A 144 MET TRP LEU GLN SER LEU LEU LEU LEU GLY THR VAL ALA
SEQRES 2 A 144 CYS SER ILE SER ALA PRO ALA ARG SER PRO SER PRO SER
SEQRES 3 A 144 THR GLN PRO TRP GLU HIS VAL ASN ALA ILE GLN GLU ALA
SEQRES 4 A 144 ARG ARG LEU LEU ASN LEU SER ARG ASP THR ALA ALA GLU
SEQRES 5 A 144 MET ASN GLU THR VAL GLU VAL ILE SER GLU MET PHE ASP
SEQRES 6 A 144 LEU GLN GLU PRO THR CYS LEU GLN THR ARG LEU GLU LEU
SEQRES 7 A 144 TYR LYS GLN GLY LEU ARG GLY SER LEU THR LYS LEU LYS
SEQRES 8 A 144 GLY PRO LEU THR MET MET ALA SER HIS TYR LYS GLN HIS
SEQRES 9 A 144 CYS PRO PRO THR PRO GLU THR SER CYS ALA THR GLN ILE
SEQRES 10 A 144 ILE THR PHE GLU SER PHE LYS GLU ASN LEU LYS ASP PHE
SEQRES 11 A 144 LEU LEU VAL ILE PRO PHE ASP CYS TRP GLU PRO VAL GLN
SEQRES 12 A 144 GLU
SEQRES 1 H 236 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN
SEQRES 2 H 236 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY
SEQRES 3 H 236 PHE THR PHE SER SER TYR TRP MET ASN TRP VAL ARG GLN
SEQRES 4 H 236 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER GLY ILE SER
SEQRES 5 H 236 TYR SER GLY SER GLU THR TYR TYR ALA ASP SER VAL LYS
SEQRES 6 H 236 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR
SEQRES 7 H 236 LEU TYR LEU GLN MET ASN SER LEU ARG ALA GLU ASP THR
SEQRES 8 H 236 ALA VAL TYR TYR CYS ALA ARG GLY PHE GLY THR ASP PHE
SEQRES 9 H 236 TRP GLY GLN GLY THR LEU VAL THR VAL SER SER ALA SER
SEQRES 10 H 236 THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER
SEQRES 11 H 236 LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU
SEQRES 12 H 236 VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP
SEQRES 13 H 236 ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO
SEQRES 14 H 236 ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SER
SEQRES 15 H 236 VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN THR
SEQRES 16 H 236 TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS
SEQRES 17 H 236 VAL ASP LYS LYS VAL GLU PRO LYS SER GLU PHE ASP TYR
SEQRES 18 H 236 LYS ASP ASP ASP ASP LYS GLY ALA PRO HIS HIS HIS HIS
SEQRES 19 H 236 HIS HIS
SEQRES 1 L 209 ASP ILE GLU LEU THR GLN PRO PRO SER VAL SER VAL ALA
SEQRES 2 L 209 PRO GLY GLN THR ALA ARG ILE SER CYS SER GLY ASP SER
SEQRES 3 L 209 ILE GLY LYS LYS TYR ALA TYR TRP TYR GLN GLN LYS PRO
SEQRES 4 L 209 GLY GLN ALA PRO VAL LEU VAL ILE TYR LYS LYS ARG PRO
SEQRES 5 L 209 SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SER GLY
SEQRES 6 L 209 ASN THR ALA THR LEU THR ILE SER GLY THR GLN ALA GLU
SEQRES 7 L 209 ASP GLU ALA ASP TYR TYR CYS SER ALA TRP GLY ASP LYS
SEQRES 8 L 209 GLY MET VAL PHE GLY GLY GLY THR LYS LEU THR VAL LEU
SEQRES 9 L 209 GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU PHE PRO
SEQRES 10 L 209 PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA THR LEU
SEQRES 11 L 209 VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA VAL THR
SEQRES 12 L 209 VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS ALA GLY
SEQRES 13 L 209 VAL GLU THR THR THR PRO SER LYS GLN SER ASN ASN LYS
SEQRES 14 L 209 TYR ALA ALA SER SER TYR LEU SER LEU THR PRO GLU GLN
SEQRES 15 L 209 TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL THR HIS
SEQRES 16 L 209 GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO THR GLU
SEQRES 17 L 209 ALA
HET PEG H 301 7
HET SO4 L 301 5
HET SO4 L 302 5
HETNAM PEG DI(HYDROXYETHYL)ETHER
HETNAM SO4 SULFATE ION
FORMUL 4 PEG C4 H10 O3
FORMUL 5 SO4 2(O4 S 2-)
FORMUL 7 HOH *198(H2 O)
HELIX 1 AA1 GLU A 14 SER A 29 1 16
HELIX 2 AA2 CYS A 54 GLY A 65 1 12
HELIX 3 AA3 LEU A 70 LYS A 72 5 3
HELIX 4 AA4 LEU A 73 CYS A 88 1 16
HELIX 5 AA5 PHE A 103 ILE A 117 1 15
HELIX 6 AA6 THR H 28 TYR H 32 5 5
HELIX 7 AA7 ARG H 83 THR H 87 5 5
HELIX 8 AA8 SER H 156 ALA H 158 5 3
HELIX 9 AA9 LYS H 201 ASN H 204 5 4
HELIX 10 AB1 SER L 27 LYS L 31 5 5
HELIX 11 AB2 GLN L 79 GLU L 83 5 5
HELIX 12 AB3 SER L 121 ALA L 127 1 7
HELIX 13 AB4 THR L 181 HIS L 188 1 8
SHEET 1 AA1 2 THR A 39 ILE A 43 0
SHEET 2 AA1 2 THR A 98 THR A 102 -1 O ILE A 101 N VAL A 40
SHEET 1 AA2 4 GLN H 3 SER H 7 0
SHEET 2 AA2 4 LEU H 18 SER H 25 -1 O SER H 21 N SER H 7
SHEET 3 AA2 4 THR H 77 MET H 82 -1 O LEU H 80 N LEU H 20
SHEET 4 AA2 4 PHE H 67 ASP H 72 -1 N THR H 68 O GLN H 81
SHEET 1 AA3 6 LEU H 11 VAL H 12 0
SHEET 2 AA3 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12
SHEET 3 AA3 6 ALA H 88 ARG H 94 -1 N ALA H 88 O VAL H 109
SHEET 4 AA3 6 MET H 34 GLN H 39 -1 N VAL H 37 O TYR H 91
SHEET 5 AA3 6 LEU H 45 ILE H 51 -1 O GLU H 46 N ARG H 38
SHEET 6 AA3 6 THR H 57 TYR H 59 -1 O TYR H 58 N GLY H 50
SHEET 1 AA4 4 SER H 120 LEU H 124 0
SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145
SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181
SHEET 1 AA5 4 SER H 120 LEU H 124 0
SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O GLY H 139 N LEU H 124
SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O TYR H 176 N TYR H 145
SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177
SHEET 1 AA6 3 THR H 151 TRP H 154 0
SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153
SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198
SHEET 1 AA7 5 SER L 9 VAL L 13 0
SHEET 2 AA7 5 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 AA7 5 ALA L 84 GLY L 92 -1 N ALA L 84 O LEU L 104
SHEET 4 AA7 5 TYR L 34 GLN L 38 -1 N GLN L 38 O ASP L 85
SHEET 5 AA7 5 VAL L 45 LEU L 46 -1 O VAL L 45 N GLN L 37
SHEET 1 AA8 4 SER L 9 VAL L 13 0
SHEET 2 AA8 4 THR L 102 VAL L 106 1 O THR L 105 N VAL L 11
SHEET 3 AA8 4 ALA L 84 GLY L 92 -1 N ALA L 84 O LEU L 104
SHEET 4 AA8 4 GLY L 95 PHE L 98 -1 O VAL L 97 N ALA L 90
SHEET 1 AA9 3 ALA L 19 SER L 24 0
SHEET 2 AA9 3 THR L 70 ILE L 75 -1 O ILE L 75 N ALA L 19
SHEET 3 AA9 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74
SHEET 1 AB1 4 SER L 114 PHE L 118 0
SHEET 2 AB1 4 ALA L 130 PHE L 139 -1 O LEU L 135 N THR L 116
SHEET 3 AB1 4 TYR L 172 LEU L 180 -1 O LEU L 180 N ALA L 130
SHEET 4 AB1 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 177
SHEET 1 AB2 4 SER L 114 PHE L 118 0
SHEET 2 AB2 4 ALA L 130 PHE L 139 -1 O LEU L 135 N THR L 116
SHEET 3 AB2 4 TYR L 172 LEU L 180 -1 O LEU L 180 N ALA L 130
SHEET 4 AB2 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 173
SHEET 1 AB3 4 SER L 153 VAL L 155 0
SHEET 2 AB3 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153
SHEET 3 AB3 4 TYR L 191 HIS L 197 -1 O GLN L 194 N ALA L 147
SHEET 4 AB3 4 SER L 200 VAL L 206 -1 O VAL L 202 N VAL L 195
SSBOND 1 CYS A 54 CYS A 96 1555 1555 2.08
SSBOND 2 CYS A 88 CYS A 121 1555 1555 2.04
SSBOND 3 CYS H 22 CYS H 92 1555 1555 2.12
SSBOND 4 CYS H 140 CYS H 196 1555 1555 2.08
SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.05
SSBOND 6 CYS L 134 CYS L 193 1555 1555 2.06
CISPEP 1 PHE H 146 PRO H 147 0 -9.84
CISPEP 2 GLU H 148 PRO H 149 0 -2.75
CISPEP 3 TYR L 140 PRO L 141 0 -1.65
SITE 1 AC1 5 PRO H 126 SER H 127 SER H 128 THR H 135
SITE 2 AC1 5 ALA H 137
SITE 1 AC2 5 ASP L 1 ILE L 2 LYS L 31 GLY L 92
SITE 2 AC2 5 ASP L 93
SITE 1 AC3 7 GLU L 83 VAL L 106 GLY L 107 GLN L 108
SITE 2 AC3 7 TYR L 140 LYS L 166 HOH L 428
CRYST1 158.680 158.680 158.680 90.00 90.00 90.00 I 21 3 24
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.006302 0.000000 0.000000 0.00000
SCALE2 0.000000 0.006302 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006302 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
